ID E9FLF4_9STRE Unreviewed; 501 AA.
AC E9FLF4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Pyruvate kinase {ECO:0000256|ARBA:ARBA00018587, ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|ARBA:ARBA00012142, ECO:0000256|RuleBase:RU000504};
GN Name=pyk {ECO:0000313|EMBL:EFX59313.1};
GN ORFNames=HMPREF0851_00285 {ECO:0000313|EMBL:EFX59313.1};
OS Streptococcus sp. M334.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=563038 {ECO:0000313|EMBL:EFX59313.1, ECO:0000313|Proteomes:UP000003840};
RN [1] {ECO:0000313|EMBL:EFX59313.1, ECO:0000313|Proteomes:UP000003840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M334 {ECO:0000313|EMBL:EFX59313.1,
RC ECO:0000313|Proteomes:UP000003840};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S., Surette M.G.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. M334.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40; Evidence={ECO:0000256|RuleBase:RU000504};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC ECO:0000256|RuleBase:RU000504}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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DR EMBL; GL732486; EFX59313.1; -; Genomic_DNA.
DR RefSeq; WP_001042787.1; NZ_GL732486.1.
DR AlphaFoldDB; E9FLF4; -.
DR eggNOG; COG0469; Bacteria.
DR HOGENOM; CLU_015439_0_2_9; -.
DR OrthoDB; 9812123at2; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000003840; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR NCBIfam; TIGR01064; pyruv_kin; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR PANTHER; PTHR11817:SF132; PYRUVATE KINASE 1; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF52935; PK C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000504};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000504};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000504};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:EFX59313.1};
KW Transferase {ECO:0000256|RuleBase:RU000504, ECO:0000313|EMBL:EFX59313.1}.
FT DOMAIN 3..353
FT /note="Pyruvate kinase barrel"
FT /evidence="ECO:0000259|Pfam:PF00224"
FT DOMAIN 387..497
FT /note="Pyruvate kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02887"
SQ SEQUENCE 501 AA; 54795 MW; F67FC21C661E14DF CRC64;
MNKRVKIVAT LGPAVEIRGG KKFGDDGYWG EKLDVEASAK NIAKLIEAGA NTFRFNFSHG
DHQEQGDRMA TVKLAEKLAG KKVGFLLDTK GPEIRTELFE GDAKEYSYKT GEKIRVATKQ
GIKSTRDVIA LNVAGALDIY DDVEVGRQVL VDDGKLGLRV VAKDDVAREF EVEVENDGII
AKQKGVNIPN TKIPFPALAE RDNDDIRFGL EQGINFIAIS FVRTAKDVNE VRAICKETGN
GHVQLFAKIE NQQGIDNLDE IIEVADGIMI ARGDMGIEVP YEMVPVYQKM IIKKVNAAGK
VVITATNMLE TMTEKPRATR SEVSDVFNAV IDGTDATMLS GESANGKYPL ESVTTMATID
KNAQTLLNEY GRLNSDSFER NSKTEVMASA VKDATNSMDI KLVVTLTKTG HTARLISKYR
PNADILALTF DELTERGLML NWGVIPMLTD APSSTDDMFE IAERKAVEAG LVQSGDDIVI
VAGVPVGEAV RTNTMRIRTV R
//
